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UniProtKB/Swiss-Prot O95479: Variant p.Arg453Gln

GDH/6PGL endoplasmic bifunctional protein
Gene: H6PD
Variant information

Variant position:  453
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  US
The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change:  From Arginine (R) to Glutamine (Q) at position 453 (R453Q, p.Arg453Gln).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from large size and basic (R) to medium size and polar (Q)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  1
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description:  In CORTRD1; unknown pathological significance; no effect on glucose-6-phosphate dehydrogenase activity; however an effect was originally observed.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  453
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  791
The length of the canonical sequence.

Location on the sequence:   PPGLRLFGSPLSDYYAYSPV  R ERDAHSVLLSHIFHGRKNFF
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.

Residue conservation: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         PPGLRLFGSPLSDYYAYSPVRERDAHSVLLSHIFHGRKNFF

Mouse                         QPGLRLFGRPLSDYYAYRPVREQDAYSTLLSHIFHCRKESF

Rabbit                        RPGLQLFGRPLSDFYAFSPVKERDAYSILLSHIFHARKESF

Sequence annotation in neighborhood:  
The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.

TypePositionsDescription
Chain 20 – 791 GDH/6PGL endoplasmic bifunctional protein
Region 20 – 526 Hexose-6-phosphate dehydrogenase


Literature citations

The full-ORF clone resource of the German cDNA consortium.
Bechtel S.; Rosenfelder H.; Duda A.; Schmidt C.P.; Ernst U.; Wellenreuther R.; Mehrle A.; Schuster C.; Bahr A.; Bloecker H.; Heubner D.; Hoerlein A.; Michel G.; Wedler H.; Koehrer K.; Ottenwaelder B.; Poustka A.; Wiemann S.; Schupp I.;
BMC Genomics 8:399-399(2007)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2); VARIANT CORTRD1 GLN-453; VARIANT ALA-151;

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]; VARIANT GLN-453;

Mutations in the genes encoding 11beta-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase interact to cause cortisone reductase deficiency.
Draper N.; Walker E.A.; Bujalska I.J.; Tomlinson J.W.; Chalder S.M.; Arlt W.; Lavery G.G.; Bedendo O.; Ray D.W.; Laing I.; Malunowicz E.; White P.C.; Hewison M.; Mason P.J.; Connell J.M.; Shackleton C.H.L.; Stewart P.M.;
Nat. Genet. 34:434-439(2003)
Cited for: VARIANT CORTRD1 GLN-453; CHARACTERIZATION OF VARIANT CORTRD1 GLN-453; FUNCTION; CATALYTIC ACTIVITY; PATHWAY;

Steroid biomarkers and genetic studies reveal inactivating mutations in hexose-6-phosphate dehydrogenase in patients with cortisone reductase deficiency.
Lavery G.G.; Walker E.A.; Tiganescu A.; Ride J.P.; Shackleton C.H.; Tomlinson J.W.; Connell J.M.; Ray D.W.; Biason-Lauber A.; Malunowicz E.M.; Arlt W.; Stewart P.M.;
J. Clin. Endocrinol. Metab. 93:3827-3832(2008)
Cited for: VARIANTS CORTRD1 316-TYR--GLY-791 DEL AND ASP-359; CHARACTERIZATION OF VARIANTS CORTRD1 316-TYR--GLY-791 DEL; ASP-359 AND GLN-453; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; SUBCELLULAR LOCATION;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.